Thyroid Peroxidase

Krinsky, Mary M.; Alexander, Natalie

doi:10.1016/s0021-9258(18)62000-9

Cited by 30 publications

(1 citation statement)

References 18 publications

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“…This indicates a hydrophobic type of interaction between the apoprotein and the prosthetic group. Similar hydrophobic or non-covalent binding between haem and protein has been reported for other haemoproteins also (Strittmatter, 1960;Feigelson & Greengard, 1961;Krinsky & Alexander, 1971). It is conceivable that acetylation of the serine residue affects the hydrophobic interaction and binding of haemin to the cyclo-oxygenase enzyme.…”

Section: Acetylation Of the Platelet Cyclo-oxygenase Bysupporting

confidence: 65%

Purification and characterization of sheep platelet cyclo-oxygenase Acetylation by aspirin prevents haemin binding to the enzyme

Boopathy¹,

Balasubramanian²

1986

Biochemical Journal

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Arachidonate cyclo-oxygenase (prostaglandin synthetase; prostaglandin endoperoxide synthetase; EC 1.14.99.1) was purified from sheep platelets. The purification procedure involved hydrophobic column chromatography using either Ibuprofen-Sepharose, phenyl-Sepharose or arachidic acid-Sepharose as the first step followed by metal-chelate Sepharose and haemin-Sepharose affinity chromatography. The purified enzyme (Mr approximately 65,000) was homogeneous as observed by SDS/polyacrylamide-gel electrophoresis and silver staining. The enzyme was a glycoprotein with mannose as the neutral sugar. Haemin or haemoglobin was essential for activity. The purified enzyme could bind haemin exhibiting a characteristic absorption maximum at 410 nm. The enzyme after metal-chelate column chromatography could undergo acetylation by [acetyl-3H]aspirin. The labelled acetylated enzyme could not bind to haemin-Sepharose, presumably due to acetylation of a serine residue involved in the binding to haemin. The acetylated enzyme also failed to show its characteristic absorption maximum at 410 nm when allowed to bind haemin.

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Section: Acetylation Of the Platelet Cyclo-oxygenase Bysupporting

confidence: 65%

Purification and characterization of sheep platelet cyclo-oxygenase Acetylation by aspirin prevents haemin binding to the enzyme

Boopathy¹,

Balasubramanian²

1986

Biochemical Journal

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Identification and Regulation of Thyroperoxidase: Use of Specific Antiserum

Pratt-Carlin

Eggo

Burrow

1986

Frontiers in Thyroidology

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Salivary peroxidases

Banerjee

Datta

1986

Mol Cell Biochem

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Peroxidases are known to be involved in the intracellular metabolism of H2O2 coupled with various physiological functions. Apart from the thyroid gland, the enzyme has been isolated from various extrathyroidal sources of which salivary gland is one of the richest sources of the enzyme. The enzyme from bovine and goat submaxillary gland has been extensively studied in terms of their molecular, spectral, kinetic, catalytic and immunological properties and compared with the lactoperoxidase which is similar to the salivary peroxidase. The modulation of the salivary peroxidase by various factors and the probable mechanism of the modulation has been described. The enzyme has also been compared with the thyroid peroxidase as regards their physicochemical properties as well as on the immunological and functional aspects. The similarities and dissimilarities have been incorporated. The possible function of the enzyme in iodine metabolism and in bactericidal action has been discussed.

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Thyroid Peroxidase

Cited by 30 publications

References 18 publications

Purification and characterization of sheep platelet cyclo-oxygenase Acetylation by aspirin prevents haemin binding to the enzyme

Purification and characterization of sheep platelet cyclo-oxygenase Acetylation by aspirin prevents haemin binding to the enzyme

Identification and Regulation of Thyroperoxidase: Use of Specific Antiserum

Salivary peroxidases

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